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Guanidine‐Ferroheme Coordination in the Mutant Protein Nitrophorin 4(L130R)
Author(s) -
He Chunmao,
Fuchs Martin R.,
Ogata Hideaki,
Knipp Markus
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201108691
Subject(s) - guanidine , deprotonation , mutant , chemistry , porphyrin , heme , chelation , coordination complex , stereochemistry , biochemistry , organic chemistry , metal , enzyme , ion , gene
Prestidigitation : In a mutant of the heme protein nitrophorin 4, the first binding of guanidine to iron in a porphyrin is observed (see structure). The protein pocket has two effects that aid this binding: its overall structure holds the ligands together providing binding energy from the chelate effect and it facilitates the deprotonation of the highly basic guanidine residue.
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